Enhanced Activity of Enzyme Immobilized on Hydrophobic ZIF‐8 Modified by Ni2+ Ions. Issue 7 (12th January 2023)

• Record Type: Journal Article
• Authors: Yang, Xiao‐Gang; Zhang, Ji‐Rui; Tian, Xu‐Ke; Qin, Jian‐Hua; Zhang, Xin‐Ya; Ma, Lu‐Fang
• Is Part Of: Angewandte Chemie international edition. Volume 62:Issue 7(2023)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2023-01-12
• Subjects: Activity -- Enzyme -- Hydrophobicity -- Immobilization -- Metal-Organic Frameworks; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.202216699
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: The development of efficient enzyme immobilization to promote their recyclability and activity is highly desirable. Zeolitic imidazolate framework‐8 (ZIF‐8) has been proved to be an effective platform for enzyme immobilization due to its easy preparation and biocompatibility. However, the intrinsic hydrophobic characteristic hinders its further development in this filed. Herein, a facile synthesis approach was developed to immobilize pepsin (PEP) on the ZIF‐8 carrier by using Ni 2+ ions as anchor (ZIF‐8@PEP‐Ni). By contrast, the direct coating of PEP on the surface of ZIF‐8 (ZIF‐8@PEP) generated significant conformational changes. Electrochemical oxygen evolution reaction (OER) was employed to study the catalytic activity of immobilized PEP. The ZIF‐8@PEP‐Ni composite attains remarkable OER performance with an ultralow overpotential of only 127 mV at 10 mA cm −2, which is much lower than the 690 and 919 mV overpotential values of ZIF‐8@PEP and PEP, respectively. Abstract : A facile synthesis approach was developed to immobilize enzyme on the ZIF‐8 carrier by using Ni 2+ ions as anchor, which can significantly promote the recyclability and activity of the enzyme.